EC Number   |
Protein Variants |
Reference |
|---|
    1.16.3.1 | A19Y |
site-directed mutagenesis, introduction of a stop codon at position 166 and replacment of Ala19 by a Tyr residue. The mutant is able to bind, oxidize and store iron, and its activity is inhibited by Zn(II) as described for other ferritins. The mutant enzymes shows reduced activity and protein stability compared to the wild-type enzyme |
-, 746386 |
| 1.16.3.1 | C35A |
putative lipidation site is dispensable for MmcO activity: mutation shows only minor impact on enzymatic activity |
-, 763203 |
| 1.16.3.1 | C486A |
cysteine 486 is required for MmcO activity. Mutation results in inactive Rv0846c protein which does not protect Mycobacterium tuberculosis against copper stress |
-, 763203 |
| 1.16.3.1 | C500S |
mutation leads to loss of the T1 copper |
-, 763245 |
| 1.16.3.1 | D278A |
normal absorbance at 330 nm and 608 nm due to type 3 and type 1 copper sites, EPR spectra equivalent to wild-type, in crease in Km-value compared to wild-type |
659524 |
| 1.16.3.1 | D283A |
wild-type reduction potential |
672085 |
| 1.16.3.1 | D283A |
X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 7-fold increase in Km value for Fe(II) |
687084 |
| 1.16.3.1 | D409A |
increase in reduction potential by 120 mV |
672085 |
| 1.16.3.1 | D409A |
X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 4-fold increase in Km value for Fe(II) |
687084 |
| 1.16.3.1 | D47A |
interactions of mutant D74A with various divalent ions compared to the wild-type enzyme, overview |
715926 |
